› 1icn

X-ray diffraction
1.74Å resolution

ESCHERICHIA COLI-DERIVED RAT INTESTINAL FATTY ACID BINDING PROTEIN WITH BOUND MYRISTATE AT 1.5 A RESOLUTION AND I-FABPARG106-->GLN WITH BOUND OLEATE AT 1.74 A RESOLUTION

Released:
DOI: 10.2210/pdb1icn/pdb
PDB entry 1icn coloured by chain, front view.
PDB entry 1icn coloured by chain, side view.
PDB entry 1icn coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Escherichia coli-derived rat intestinal fatty acid binding protein with bound myristate at 1.5 A resolution and I-FABPArg106-->Gln with bound oleate at 1.74 A resolution.
Eads J, Sacchettini JC, Kromminga A, Gordon JI
J Biol Chem 268 26375-85 (1993)
PMID: 8253762

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid-binding protein, intestinal Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.99 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: P02693 (Residues: 2-132; Coverage: 99%)
Gene names: Fabp2, Fabpi
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand OLA 1 x OLA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 35.82Å b: 51.55Å c: 31.24Å
α: 90° β: 92.28° γ: 90°
R-values:
R R work R free
0.161 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Cellular fatty acid-binding proteins: their function and physiological significance.
Glatz et al. (1996)
2 more

8 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
7 more